ID K8EA98_9CHLO Unreviewed; 773 AA.
AC K8EA98;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=Bathy01g02720 {ECO:0000313|EMBL:CCO14614.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO14614.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO14614.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO14614.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR EMBL; FO082278; CCO14614.1; -; Genomic_DNA.
DR RefSeq; XP_007515735.1; XM_007515673.1.
DR AlphaFoldDB; K8EA98; -.
DR STRING; 41875.K8EA98; -.
DR GeneID; 19018007; -.
DR KEGG; bpg:Bathy01g02720; -.
DR eggNOG; KOG0136; Eukaryota.
DR OrthoDB; 5473219at2759; -.
DR Proteomes; UP000198341; Chromosome_1.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 55..212
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 579..753
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 520
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 773 AA; 85475 MW; 7D27C3DA5C30B6BA CRC64;
MNTAWKSEST NEAEADEDDI TLARKLQTPV SKQIAQSSVD PRKDLLRERE RASFNSRELE
VLLAGGVENV KLRKLVAETL TKDRVFKNKT SEKYSLPREE LYRTTLEKYL EIPRVAREIL
AKIHGDNGGG GGGGSGGGAT RSRSGNSGDS GNGVNKSNNN KLIAIARVVR EFIDEPGGLD
LHLGMFIPTI QGQGTDEQKK YWLPKCVNLE IVGTYAQTEL GHGTFIRGLE TTCTYDVRKK
EFIVHSPTLT ATKWWPGGLG KTATHAIVMA RLFVPSSSSS SSSFASHSEP VFSDKGIHAF
VVQIRSTKDH LPLPGVQCGD IGDKMGYNAV DNGFLRFDHV RVPKDAMLMG HSKVLDDGTY
VPPPVKKAAY GTMVFVRSDI VMNAALYMKK AVTIALRYNL VRRQSNADSK NNNVETQVLD
YQHSQRTLFP ILASSFAFHT TSDYMRRMYF EFLKRSQSSE KDFDALPELH ATSSGLKAFC
SWKTKDAIES CRLTCGGHGY LANAGFGTTF ASYAPNVTYE GDNNVLCLQT SRYLLKTMRA
LQAKLVTEVK LVGQMKYLSE SGNTFTSTLG HEVGIRDEDA LLRAYEHRAW RLCSQATARA
GNLSVDEAMR LDMVSWIKVA KSHCALVVLA NFFDGIHEAE KLKVSKETIA VLKRLATLHA
LCGVEDELGD WVEDGYLEAM QCQLVREEIA QLLQELRPDA AALADSLGLD DYFLNSTLGA
RDGNVYENLF AAAQKAPFNS SHKPPGYDHL LWPRFNASSN SNTSNNNKGR SKL
//
